ID   ECTD_NOCFA              Reviewed;         298 AA.
AC   Q5YW75;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Ectoine dioxygenase {ECO:0000250|UniProtKB:Q2TDY4};
DE            EC=1.14.11.55 {ECO:0000250|UniProtKB:Q2TDY4};
DE   AltName: Full=Ectoine hydroxylase {ECO:0000250|UniProtKB:Q2TDY4};
GN   Name=ectD {ECO:0000250|UniProtKB:Q2TDY4}; OrderedLocusNames=NFA_27190;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of 5-hydroxyectoine, called
CC       compatible solute, which helps organisms to survive extreme osmotic
CC       stress by acting as a highly soluble organic osmolyte. Catalyzes the 2-
CC       oxoglutarate-dependent selective hydroxylation of L-ectoine to yield
CC       (4S,5S)-5-hydroxyectoine. {ECO:0000250|UniProtKB:Q2TDY4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-ectoine + O2 = 5-hydroxyectoine + CO2 +
CC         succinate; Xref=Rhea:RHEA:45740, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58515, ChEBI:CHEBI:85413; EC=1.14.11.55;
CC         Evidence={ECO:0000250|UniProtKB:Q2TDY4};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q2TDY4};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000250|UniProtKB:Q2TDY4};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q2TDY4}.
CC   -!- SIMILARITY: Belongs to the PhyH family. EctD subfamily.
CC       {ECO:0000250|UniProtKB:Q2TDY4}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP006618; BAD57566.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5YW75; -.
DR   SMR; Q5YW75; -.
DR   STRING; 247156.NFA_27190; -.
DR   EnsemblBacteria; BAD57566; BAD57566; NFA_27190.
DR   KEGG; nfa:NFA_27190; -.
DR   eggNOG; COG5285; Bacteria.
DR   HOGENOM; CLU_048953_5_0_11; -.
DR   OMA; FPRSNVF; -.
DR   Proteomes; UP000006820; Chromosome.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0042400; P:ectoine catabolic process; ISS:UniProtKB.
DR   InterPro; IPR012774; EctD.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
DR   TIGRFAMs; TIGR02408; ectoine_ThpD; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..298
FT                   /note="Ectoine dioxygenase"
FT                   /id="PRO_0000215240"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133
FT                   /ligand="L-ectoine"
FT                   /ligand_id="ChEBI:CHEBI:58515"
FT                   /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT   BINDING         150
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   BINDING         152
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   BINDING         251
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   SITE            156
FT                   /note="Important for ectoine stabilization"
FT                   /evidence="ECO:0000250|UniProtKB:Q1GNW5"
SQ   SEQUENCE   298 AA;  33480 MW;  C98765BD70E75DD9 CRC64;
     MLQQAIDRDP VDRIDRYPTR TAEPAPHIER LDPTVWGEVH SEQLSTFDRD GFSIMENLLS
     PEEVSEFRAE VERLAADKSL LDDERVIREK TSNRVRSVFE VHKLSAAVAD LVRQTRIVGL
     ARQVLGSDVY LHQTRINYMP GFRGTGFYWH SDFETWHAED GMPAPRAVSL SIALTDNYPF
     NGSLMVMPGS HRTFVPCVGA TPADHYRESL REQEIGVPST EDITVLAQRY GITQFTGRAG
     SALLFDSNVM HGSANNITPF PRSNIFLVFN SVENTLVEPF AAPAPRPTYI GSRDFTPL